UID:
almafu_9958129887202883
Format:
1 online resource (824 p.)
ISBN:
9786610635818
,
9781280635816
,
1280635819
,
9780080463599
,
0080463592
Series Statement:
Methods in enzymology ; v. 407
Content:
The Ras superfamily (〉150 human members) encompasses Ras GTPases involved in cell proliferation, Rho GTPases involved in regulating the cytoskeleton, Rab GTPases involved in membrane targeting/fusion and a group of GTPases including Sar1, Arf, Arl and dynamin involved in vesicle budding/fission. These GTPases act as molecular switches and their activities are controlled by a large number of regulatory molecules that affect either GTP loading (guanine nucleotide exchange factors or GEFs) or GTP hydrolysis (GTPase activating proteins or GAPs). In their active state, they interact with a continua
Note:
Description based upon print version of record.
,
Cover Page; Table of Contents; Contributors to Volume 407; Preface; Volumes in Series; Chapter 1: Ras Superfamily and Interacting Proteins Database; Introduction; A Database of Ras Superfamily Proteins and Their Regulators; References; Chapter 2: Real-Time In Vitro Measurement of Intrinsic and Ras GAP-Mediated GTP Hydrolysis; Introduction; Experimental Procedures; Data Analysis; Concluding Remarks; References; Chapter 3: Schwann Cell Preparation from Single Mouse Embryos: Analyses of Neurofibromin Function in Schwann Cells; Introduction; Materials and Methods
,
Characterization of Phenotypes of Schwann Cells Derived from Wild-Type and Nf1 Mutant MiceSummary; Acknowledgments; References; Chapter 4: Regulation of the Nucleotide State of Oncogenic Ras Proteins by Nucleoside Diphosphate Kinase; Introduction; Methods; Establishing a ""Medium-Throughput"" GTPase Activity Assay; Detection of Protein-Bound Nucleotides by 96-Well Vacuum Filtration; Detection of Protein-Bound Nucleotides by Thin-Layer Chromatography; Characterization of a Bacterial Lysate Component with GTPase-Stimulating Activity
,
Purification and Identification of the Protein Responsible for Lysate ActivityNDK Is the E. coli Protein Responsible for Inactivation of Oncogenic Ras; GTPase-Inactivating Activity of NDK Is Specific to Mutant Ras Enzymes; Nucleotides Do Not Detectably Dissociate from Ras During the Reaction with NDK; NDK Catalyzes the Reverse Reaction: Conversion of Ras-GDP to Ras-GTP; Conclusions; Acknowledgments; References; Chapter 5: Measurements of TSC2 GAP Activity Toward Rheb; Introduction; In Vitro Assay of TSC2 GAP Stimulated Rheb GTP Hydrolysis; TSC2 GAP-Stimulated Rheb GTP Hydrolysis In Vivo
,
TSC2 Inhibits the Phosphorylation of Thr-389 of S6K1Conclusion and Discussion; References; Chapter 6: Characterization of AND-34 Function and Signaling; Overview; Retrovirus-Mediated Analysis of AND-34-Induced Cdc42 Activation in Lymphoid Cell Lines; AND-34-Induced Cdc42 and Rac Activation in MCF-7 Cells; PAK1 and Akt Kinase Assays; Measurement of R-Ras GTP Levels; Acknowledgments; References; Chapter 7: Studying the Spatial and Temporal Regulation of Ras GTPase-Activating Proteins; Introduction; Methods; Conclusion; Acknowledgments; References
,
Chapter 8: Activation of Ras Proteins by Ras Guanine Nucleotide Releasing Protein Family MembersIntroduction; Ras Guanine Nucleotide Releasing Proteins (RasGRPs); Analysis of RasGRP Protein Activity in Cells; Concluding Remarks; References; Chapter 9: Ras and Rap1 Activation of PLCepsiv Lipase Activity; Introduction; Methods; References; Chapter 10: Specificity and Expression of RalGPS as RalGEFs; Background; Expression of RalGPS1A/B in 293T Cells; Production and Purification of GST Fusion Proteins; Ras Protein Binding Assay; SH3 Binding Assays; In Vivo Exchange Assay
,
Subcellular Fractionation
Additional Edition:
ISBN 9780121828127
Additional Edition:
ISBN 0121828123
Language:
English
Bookmarklink
